RAB13_BOVIN
ID RAB13_BOVIN Reviewed; 203 AA.
AC Q58DS5; Q32KZ4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ras-related protein Rab-13;
DE Flags: Precursor;
GN Name=RAB13;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH PRKACA.
RX PubMed=15096524; DOI=10.1083/jcb.200312118;
RA Koehler K., Louvard D., Zahraoui A.;
RT "Rab13 regulates PKA signaling during tight junction assembly.";
RL J. Cell Biol. 165:175-180(2004).
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different sets of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab is involved in
CC endocytic recycling and regulates the transport to the plasma membrane
CC of transmembrane proteins like the tight junction protein
CC OCLN/occludin. Thereby, it regulates the assembly and the activity of
CC tight junctions. Moreover, it may also regulate tight junction assembly
CC by activating the PKA signaling pathway and by reorganizing the actin
CC cytoskeleton through the activation of the downstream effectors PRKACA
CC and MICALL2 respectively. Through its role in tight junction assembly,
CC may play a role in the establishment of Sertoli cell barrier. Plays
CC also a role in angiogenesis through regulation of endothelial cells
CC chemotaxis. Also involved in neurite outgrowth. Has also been proposed
CC to play a role in post-Golgi membrane trafficking from the TGN to the
CC recycling endosome. Finally, it has been involved in insulin-induced
CC transport to the plasma membrane of the glucose transporter GLUT4 and
CC therefore may play a role in glucose homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:P51153}.
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP). That Rab may be
CC activated by DENND1C, a guanine exchange factor. Activated in response
CC to insulin (By similarity). {ECO:0000250|UniProtKB:P51153}.
CC -!- SUBUNIT: Interacts (GTP-bound form) with MICALL2; competes with RAB8A
CC and is involved in tight junctions assembly. Interacts (GTP-bound form)
CC with MICALL1. Interacts (GTP-bound form) with MICAL1, MICAL3, MICALCL,
CC EHBP1 and EHBP1L1; ternary complexes of RAB8A, RAB13 and either MICAL1
CC or EHBP1L1 are possible. Interacts with PRKACA; downstream effector of
CC RAB13 involved in tight junction assembly. Interacts with GRB2; may
CC recruit RAB13 to the leading edge of migrating endothelial cells where
CC it can activate RHOA. Interacts (isoprenylated form) with PDE6D;
CC dissociates RAB13 from membranes. Interacts with BICDL2/BICDR2.
CC Interacts with LEPROT and LEPROTL1. {ECO:0000250|UniProtKB:P51153,
CC ECO:0000269|PubMed:15096524}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51153};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:P51153}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell junction, tight
CC junction {ECO:0000250|UniProtKB:P51153}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000250|UniProtKB:P51153}. Recycling endosome
CC membrane {ECO:0000250|UniProtKB:P51153}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q9DD03}. Note=Tight junctions or associated with
CC vesicles scattered throughout the cytoplasm in cells lacking tight
CC junctions (By similarity). Relocalizes to the leading edge of
CC lamellipodia in migrating endothelial cells (By similarity).
CC {ECO:0000250|UniProtKB:P51153, ECO:0000250|UniProtKB:Q9DD03}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BT021522; AAX46369.1; -; mRNA.
DR EMBL; BC109840; AAI09841.1; -; mRNA.
DR RefSeq; NP_001019711.1; NM_001024540.1.
DR AlphaFoldDB; Q58DS5; -.
DR SMR; Q58DS5; -.
DR STRING; 9913.ENSBTAP00000023407; -.
DR PaxDb; Q58DS5; -.
DR PRIDE; Q58DS5; -.
DR GeneID; 514541; -.
DR KEGG; bta:514541; -.
DR CTD; 5872; -.
DR eggNOG; KOG0078; Eukaryota.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q58DS5; -.
DR OrthoDB; 1426655at2759; -.
DR TreeFam; TF314097; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0010737; P:protein kinase A signaling; ISS:UniProtKB.
DR GO; GO:1902463; P:protein localization to cell leading edge; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0044795; P:trans-Golgi network to recycling endosome transport; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Endosome; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Tight junction; Transport.
FT CHAIN 1..200
FT /note="Ras-related protein Rab-13"
FT /id="PRO_0000226292"
FT PROPEP 201..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370755"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 200
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P51153"
FT CONFLICT 46
FT /note="R -> K (in Ref. 2; AAI09841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 22970 MW; 6B0C2C32DBEB942F CRC64;
MAKAYDHLFK LLLIGDSGVG KTCLIIRFAE DNFNNTYIST IGIDFRIRTV DIEGKKIKLQ
VWDTAGQERF KTITTAYYRG AMGIILVYDI TDEKSFENIQ NWMKSIKENA SAGVERLLLG
NKCDMEAKRK VQKEQADKLA REHGIRFFET SAKSSMNVDE AFSSLARDIL LKSGGRRLKN
NNKPPSTDLK TCDKKNTNKC SLA
